Endoplasmic reticulum (ER) is the site of synthesis and folding of secretory proteins.
Perturbations of ER homeostasis affect protein folding and cause ER stress. ER can sense …

Cells can respond to stress in various ways ranging from the activation of survival pathways
to the initiation of cell death that eventually eliminates damaged cells. Whether cells mount a …

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) represents a
cellular stress induced by multiple stimuli and pathological conditions. These include …

Alpha-synuclein (αSyn) misfolding is associated with several devastating
neurodegenerative disorders, including Parkinson's disease (PD). In yeast cells and in …

Proteins synthesized in the endoplasmic reticulum (ER) are properly folded with the
assistance of ER chaperones. Malfolded proteins are disposed of by ER‐associated protein …

notwithstanding the many strengths of the dynamic developmental theory, there remain
challenges to be overcome before it can be incorporated into a true causal model of …

The extracellular space is an environment hostile to unmodified polypeptides. For this
reason, many eukaryotic proteins destined for exposure to this environment through …

Endoplasmic reticulum (ER) stress is caused by disturbances in the structure and function of
the ER with the accumulation of misfolded proteins and alterations in the calcium …

Stress proteins located in the cytosol or endoplasmic reticulum (ER) maintain cell
homeostasis and afford tolerance to severe insults,,. In neurodegenerative diseases, several …

The unfolded protein response (UPR) is a stress response of the endoplasmic reticulum
(ER) to a disturbance in protein folding. The so-called ER stress sensors PERK, IRE1 and …